BACKGROUNDS: The process of amyloid proteins aggregation
causes several human neuropathologies. In some cases, e.g.
fibrillar deposits of insulin, the problems are generated in
the processes of production and purification of protein and in
the pump devices or injectable preparations for diabetics.
Experimental kinetics and adequate modelling of chemical
inhibition from amyloid aggregation are of practical importance
in order to study the viable processing, formulation and
storage as well as to predict and optimize the best conditions
to reduce the effect of protein nucleation. RESULTS: In this
manuscript, experimental data of insulin, A?42 amyloid protein
and apomyoglobin fibrillation from recent bibliography were
selected to evaluate the capability of a bivariate sigmoid
equation to model them. The mathematical functions (logistic
combined with Weibull equation) were used in reparameterized
form and the effect of inhibitor concentrations on kinetic
parameters from logistic equation were perfectly defined and
explained. The surfaces of data were accurately described by
proposed model and the presented analysis characterized the
inhibitory influence on the protein aggregation by several
chemicals. Discrimination between true and apparent inhibitors
was also confirmed by the bivariate equation. EGCG for insulin
(working at pH?=?7.4/T?=?37°C) and taiwaniaflavone for
A?42 were the compounds studied that shown the greatest
inhibition capacity. CONCLUSIONS: An accurate, simple and
effective model to investigate the inhibition of chemicals on
amyloid protein aggregation has been developed. The equation
could be useful for the clear quantification of inhibitor
potential of chemicals and rigorous comparison among them.

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